Samo Ribarič (Avtor)

Povzetek

Intracellular synthesis, folding, trafficking and degradation of proteins are controlled and integrated by proteostasis. The frequency of protein misfolding disorders in the human population, e.g., in Alzheimer's disease (AD), is increasing due to the aging population. AD treatment options are limited to symptomatic interventions that at best slow-down disease progression. The key biochemical change in AD is the excessive accumulation of per-se non-toxic and soluble amyloid peptides (A[beta](1-37/44), in the intracellular and extracellular space, that alters proteostasis and triggers A[beta] modification (e.g., by reactive oxygen species (ROS)) into toxic intermediate, misfolded soluble A[beta] peptides, A[beta] dimers and A[beta] oligomers. The toxic intermediate A[beta] products aggregate into progressively less toxic and less soluble protofibrils, fibrils and senile plaques. This review focuses on peptides that inhibit toxic A[beta] oligomerization, A[beta] aggregation into fibrils, or stabilize A[beta] peptides in non-toxic oligomers, and discusses their potential for AD treatment

Ključne besede

Alzheimer's disease;amyloid [beta] oligomers;amyloid [beta] peptide;

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.02 - Pregledni znanstveni članek
Organizacija: UL MF - Medicinska fakulteta
UDK: 616.8
COBISS: 33689817 Povezava se bo odprla v novem oknu
ISSN: 1420-3049
Št. ogledov: 209
Št. prenosov: 72
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: Alzheimerjeva bolezen;amiloidni [beta] oligomeri;amiloidni peptid;
Vrsta dela (COBISS): Članek v reviji
Strani: str. [1]-31
Letnik: ǂVol. ǂ23
Zvezek: ǂno. ǂ2
Čas izdaje: Jan. 2018
DOI: 10.3390/molecules23020283
ID: 13641453